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Q9NZV5 (SELN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Selenoprotein N

Short name=SelN
Gene names
Name:SEPN1
Synonyms:SELN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length590 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Isoform 2: Endoplasmic reticulum membrane Probable. Note: Probably membrane-associated. Ref.5

Tissue specificity

Isoform 1 and isoform 2 are expressed in skeletal muscle, brain, lung and placenta. Isoform 2 is also expressed in heart, diaphragm and stomach. Ref.1 Ref.5

Domain

The N-terminus (first 61 amino acids) contains an endoplasmic reticulum addressing and retention targeting signal.

Post-translational modification

N-glycosylated (isoform 2)

Involvement in disease

Rigid spine muscular dystrophy 1 (RSMD1) [MIM:602771]: A neuromuscular disorder characterized by poor axial muscle strength, scoliosis and neck weakness, and a variable degree of spinal rigidity. Early ventilatory insufficiency can lead to death by respiratory failure.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.6 Ref.7 Ref.8

Sequence similarities

Contains 1 EF-hand domain.

Sequence caution

The sequence AAH15638.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH42154.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Selenocysteine
   DiseaseDesmin-related myopathy
Disease mutation
Myofibrillar myopathy
   DomainSignal
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCK1P163332EBI-1751965,EBI-389883

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NZV5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: The UGA codons present in position 127 and 462 are either a selenocysteine or a real stop codon.
Isoform 2 (identifier: Q9NZV5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     102-135: Missing.
Note: The UGA codon present in position 462 is either a selenocysteine or a real stop codon.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4343 Potential
Chain44 – 590547Selenoprotein N
PRO_0000022311

Regions

Domain67 – 10236EF-hand
Compositional bias17 – 5943Ala-rich

Amino acid modifications

Non-standard residue1271Selenocysteine
Non-standard residue4621Selenocysteine
Glycosylation1261N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation4831N-linked (GlcNAc...) Potential
Glycosylation5051N-linked (GlcNAc...) Potential
Glycosylation5311N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence102 – 13534Missing in isoform 2.
VSP_011372
Natural variant1371T → A.
Corresponds to variant rs35019869 [ dbSNP | Ensembl ].
VAR_038845
Natural variant1421C → Y. Ref.1
Corresponds to variant rs7349185 [ dbSNP | Ensembl ].
VAR_038846
Natural variant2731G → E in RSMD1. Ref.1
VAR_019635
Natural variant2931H → R in RSMD1. Ref.1 Ref.6
VAR_019636
Natural variant3151G → S in RSMD1. Ref.6 Ref.7
VAR_019637
Natural variant3401N → I in RSMD1. Ref.6
VAR_019638
Natural variant4531W → S in RSMD1. Ref.6
VAR_019639
Natural variant4621U → G in RSMD1. Ref.6
VAR_019640
Natural variant4631G → V in RSMD1. Ref.8
VAR_058462
Natural variant4661R → Q in RSMD1. Ref.1 Ref.6 Ref.8
VAR_019641
Natural variant4691R → Q in RSMD1. Ref.8
VAR_058463
Natural variant4691R → W in RSMD1. Ref.8
VAR_058464
Natural variant5021N → K. Ref.1 Ref.3 Ref.4
Corresponds to variant rs2294228 [ dbSNP | Ensembl ].
VAR_038847

Experimental info

Sequence conflict2471G → S in AAF21430. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 5.
Checksum: D7D4D6331652C359

FASTA59065,813
        10         20         30         40         50         60 
MGRARPGQRG PPSPGPAAQP PAPPRRRARS LALLGALLAA AAAAAVRVCA RHAEAQAAAR 

        70         80         90        100        110        120 
QELALKTLGT DGLFLFSSLD TDGDMYISPE EFKPIAEKLT GSCSVTQTGV QWCSHSSLQP 

       130        140        150        160        170        180 
QLPWLNUSSC LSLLRSTPAA SCEEEELPPD PSEETLTIEA RFQPLLPETM TKSKDGFLGV 

       190        200        210        220        230        240 
SRLALSGLRN WTAAASPSAV FATRHFQPFL PPPGQELGEP WWIIPSELSM FTGYLSNNRF 

       250        260        270        280        290        300 
YPPPPKGKEV IIHRLLSMFH PRPFVKTRFA PQGAVACLTA ISDFYYTVMF RIHAEFQLSE 

       310        320        330        340        350        360 
PPDFPFWFSP AQFTGHIILS KDATHVRDFR LFVPNHRSLN VDMEWLYGAS ESSNMEVDIG 

       370        380        390        400        410        420 
YIPQMELEAT GPSVPSVILD EDGSMIDSHL PSGEPLQFVF EEIKWQQELS WEEAARRLEV 

       430        440        450        460        470        480 
AMYPFKKVSY LPFTEAFDRA KAENKLVHSI LLWGALDDQS CUGSGRTLRE TVLESSPILT 

       490        500        510        520        530        540 
LLNESFISTW SLVKELEELQ NNQENSSHQK LAGLHLEKYS FPVEMMICLP NGTVVHHINA 

       550        560        570        580        590 
NYFLDITSVK PEEIESNLFS FSSTFEDPST ATYMQFLKEG LRRGLPLLQP 

« Hide

Isoform 2 [UniParc].

Checksum: 0DAF9C344FA543AC
Show »

FASTA55662,034

References

« Hide 'large scale' references
[1]"Mutations in SEPN1 cause congenital muscular dystrophy with spinal rigidity and restrictive respiratory syndrome."
Moghadaszadeh B., Petit N., Jaillard C., Brockington M., Roy S.Q., Merlini L., Romero N., Estournet B., Desguerre I., Chaigne D., Muntoni F., Topaloglu H., Guicheney P.
Nat. Genet. 29:17-18(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANTS RSMD1 GLU-273; ARG-293 AND GLN-466, VARIANTS TYR-142 AND LYS-502, TISSUE SPECIFICITY.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Novel selenoproteins identified in silico and in vivo by using a conserved RNA structural motif."
Lescure A., Gautheret D., Carbon P., Krol A.
J. Biol. Chem. 274:38147-38154(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 86-590 (ISOFORM 2), VARIANT LYS-502.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 428-590 (ISOFORMS 1/2), VARIANT LYS-502.
Tissue: Lung.
[5]"Selenoprotein N: an endoplasmic reticulum glycoprotein with an early developmental expression pattern."
Petit N., Lescure A., Rederstorff M., Krol A., Moghadaszadeh B., Wewer U.M., Guicheney P.
Hum. Mol. Genet. 12:1045-1053(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]"Mutations of the selenoprotein N gene, which is implicated in rigid spine muscular dystrophy, cause the classical phenotype of multiminicore disease: reassessing the nosology of early-onset myopathies."
Ferreiro A., Quijano-Roy S., Pichereau C., Moghadaszadeh B., Goemans N., Boennemann C., Jungbluth H., Straub V., Villanova M., Leroy J.-P., Romero N.B., Martin J.-J., Muntoni F., Voit T., Estournet B., Richard P., Fardeau M., Guicheney P.
Am. J. Hum. Genet. 71:739-749(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RSMD1 ARG-293; SER-315; ILE-340; SER-453; GLY-462 AND GLN-466.
[7]"Desmin-related myopathy with Mallory body-like inclusions is caused by mutations of the selenoprotein N gene."
Ferreiro A., Ceuterick-de Groote C., Marks J.J., Goemans N., Schreiber G., Hanefeld F., Fardeau M., Martin J.-J., Goebel H.H., Richard P., Guicheney P., Bonnemann C.G.
Ann. Neurol. 55:676-686(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RSMD1 SER-315.
[8]"A mutation in the SEPN1 selenocysteine redefinition element (SRE) reduces selenocysteine incorporation and leads to SEPN1-related myopathy."
Maiti B., Arbogast S., Allamand V., Moyle M.W., Anderson C.B., Richard P., Guicheney P., Ferreiro A., Flanigan K.M., Howard M.T.
Hum. Mutat. 30:411-416(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RSMD1 VAL-463; GLN-466; GLN-469 AND TRP-469.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ306399 mRNA. Translation: CAC83791.1.
AJ306398 Genomic DNA. Translation: CAC83790.1.
AL020996 Genomic DNA. No translation available.
AF166125 mRNA. Translation: AAF21430.1.
BC015638 mRNA. Translation: AAH15638.1. Different initiation.
BC042154 mRNA. Translation: AAH42154.1. Different initiation.
RefSeqNP_065184.2. NM_020451.2.
NP_996809.1. NM_206926.1.
UniGeneHs.323396.

3D structure databases

ProteinModelPortalQ9NZV5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121439. 2 interactions.
IntActQ9NZV5. 5 interactions.
STRING9606.ENSP00000355141.

PTM databases

PhosphoSiteQ9NZV5.

Polymorphism databases

DMDM317373588.

Proteomic databases

PaxDbQ9NZV5.
PRIDEQ9NZV5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361547; ENSP00000355141; ENSG00000162430. [Q9NZV5-1]
ENST00000374315; ENSP00000363434; ENSG00000162430. [Q9NZV5-2]
GeneID57190.
KEGGhsa:57190.
UCSCuc021ojk.1. human. [Q9NZV5-1]
uc021ojl.1. human. [Q9NZV5-2]

Organism-specific databases

CTD57190.
GeneCardsGC01P026126.
HGNCHGNC:15999. SEPN1.
HPAHPA058076.
MIM602771. phenotype.
606210. gene.
neXtProtNX_Q9NZV5.
Orphanet324604. Classic multiminicore myopathy.
2020. Congenital fiber-type disproportion myopathy.
84132. Desmin-related myopathy with Mallory body-like inclusions.
97244. Rigid spine syndrome.
PharmGKBPA38079.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG68411.
HOGENOMHOG000007489.
HOVERGENHBG108469.
OMAPQGTVAC.
OrthoDBEOG7HTHGM.
PhylomeDBQ9NZV5.
TreeFamTF329622.

Gene expression databases

ArrayExpressQ9NZV5.
BgeeQ9NZV5.
CleanExHS_SEPN1.
GenevestigatorQ9NZV5.

Family and domain databases

InterProIPR002048. EF_hand_dom.
[Graphical view]
PROSITEPS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSEPN1. human.
GeneWikiSEPN1.
GenomeRNAi57190.
NextBio63268.
PROQ9NZV5.
SOURCESearch...

Entry information

Entry nameSELN_HUMAN
AccessionPrimary (citable) accession number: Q9NZV5
Secondary accession number(s): A6NJG8 expand/collapse secondary AC list , A8MQ64, Q6PI70, Q969F6, Q9NUI6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 112 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM